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C4785 Sigma

Collagenase from Clostridium histolyticum

sterile-filtered, release of physiologically active rat pancreatic islets tested, Type XI-S, 2-5 FALGPA units/mg solid, >1200 CDU/mg solid

Synonym: Clostridiopeptidase A

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Cell Dissociation,
sterility   sterile-filtered
form   lyophilized powder
suitability   release of physiologically active rat pancreatic islets tested
storage temp.   −20°C

Description

Biochem/physiol Actions

Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(beta-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, beta-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline.

Effective release of cells from tissue requires the action of collagenase enzymes and the neutral protease. Collagenase is activated by four gram atom calcium (Ca2+) per mole enzyme. The culture filtrate is thought to contain at least 7 different proteases ranging in molecular weight from 68-130 kDa. The pH optimum is 6.3-8.8. The enzyme is typically used to digest the connective components in tissue samples to liberate individual cells. Collagenase treatment can cause some cells to die. Typically, concentrations varying from 0.1 to 5 mg/mL are used for digestion. The duration of reaction varies from 15 minutes to several hours and yields a satisfactory efficiency of cell dissociation without causing too much cell death. Krebs Ringer buffer with calcium and BSA is preferred and Zn2+ is required for activity. This enzyme is tested for suitability for the release of hepatocytes (at approx. 1 mg/mL in a total volume of 100 mL) for each rat liver.

Preparation Note

Also contains clostripain, nonspecific neutral protease, and tryptic activities.

Prepared from Type XI (C7657)

Unit Definition

One collagen digestion unit (CDU) liberates peptides from collagen from bovine achilles tendon equivalent in ninhydrin color to 1.0 μmole of leucine in 5 hours at pH 7.4 at 37 °C in the presence of calcium ions. One FALGPA hydrolysis unit hydrolyzes 1.0 μmole of furylacryloyl-Leu-Gly-Pro-Ala per min at 25°C. One Neutral Protease unit hydrolyzes casein to produce color equivalent to 1.0 μmole of tyrosine per 5 hr at pH 7.5 at 37°C. One Clostripain Unit hydrolyzes 1.0 μmole of BAEE per min at pH 7.6 at 25°C in the presence of DTT.

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Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Articles

Enzymes for Cell Detachment and Tissue Dissociation

Collagenase cleaves the peptide bonds in native, triple-helical collagen. Because of its unique ability to hydrolyze native collagen, it is widely used in isolation of cells from animal tissue. Colla...
BioFiles 2006, 1.2, 3.
Keywords: Anaerobic, Biochemistry, Biofiles, Cell biology, Cell culture, Diabetes, Digestions, Enzyme activity, Fermentation, Methods, Oxidations, Purification, Type

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Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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Description

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F5135 N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala

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